InterPro: IPR016181 Acyl-CoA N-acyltransferase

This entry represents a structural domain found in several acyl-CoA acyltransferase enzymes. This domain has a 3-layer alpha/beta/alpha structure that contains mixed beta-sheets, and can be found in the following proteins:

• N-acetyl transferase (NAT) family members, including aminoglycoside N-acetyltransferases [1], the histone acetyltransferase domain of P300/CBP associating factor PCAF [2], the catalytic domain of GCN5 histone acetyltransferase [3], and diamine acetyltransferase 1 [4].
• Autoinducer synthetases, such as protein LasI [5] and acyl-homoserinelactone synthase EsaI [6].
• Leucyl/phenylalanyl-tRNA-protein transferase (LFTR), a close relative of the non-ribosomal peptidyltransferases; there is a deletion of the N-terminal half of the N-terminal NAT-like domain after the domain duplication/swapping events [7].
• Ornithine decarboxylase antizyme, which may have evolved a different function for this domain, although the putative active site maps to the same location in the common fold.
• Arginine N-succinyltransferase, alpha chain, AstA, which contains an extra C-terminal domain that is similar to the double psi beta-barrel fold domain (missing one strand and untangled psi-loops).

Several proteins carry a duplication of this domain, which consists of two NAT-like domains swapped with the C-terminal strands, including:

• N-myristoyl transferase (NMT) [8].
• FemXAB nonribosomal peptidyltransferases, including methicillin-resistance protein FemA (transfer glycyl residue from tRNA-Gly) [9] and peptidyltransferase FemX [10].
• Hypothetical protein cg14615-pa from Drosophila melanogaster (Fruit fly).